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. Author manuscript; available in PMC: 2024 May 20.
Published in final edited form as: ACS Chem Biol. 2020 Dec 4;15(12):3159–3166. doi: 10.1021/acschembio.0c00676

Figure 1.

Figure 1.

Pre-steady-state kinetic analysis of substrate binding and processing under multiple turnover conditions. (A) Stopped-flow transients monitoring OH-AA formation after mixing HsKYNase with 500 μM OH-KYN. (B) OH-AA monitored by stopped-flow after mixing HsKYNase with different concentrations of OH-KYN. Simulated traces are shown as smooth curves. (C) Fluorescent traces of anthranilate formation monitored after mixing 25 μM HsKYNase with different concentrations of KYN as shown; the inset shows the rates as a function of KYN concentration (see SI). (D) Stopped-flow fluorescent trace of the AA burst after mixing 5 μM PfKYNase with 800 μM KYN. (E) Fluorescent traces of AA formation after mixing PfKYNase with different concentrations of KYN. (F) Stopped-flow fluorescent trace of the OH-AA formation after mixing 25 μM PfKYNase with 500 μM OH-KYN. In all plots, each trace represents the average of five different measurements.